title: Binding of human milk to pathogen receptor DC-SIGN varies with bile salt-stimulated lipase (BSSL) gene polymorphism.
abstract: OBJECTIVE
  Dendritic cells bind an array of antigens and DC-SIGN has been postulated to act as a receptor for mucosal pathogen transmission. Bile salt-stimulated lipase (BSSL) from human milk potently binds DC-SIGN and blocks DC-SIGN mediated trans-infection of CD4(+) T-lymphocytes with HIV-1. Objective was to study variation in DC-SIGN binding properties and the relation between DC-SIGN binding capacity of milk and BSSL gene polymorphisms.
  
  
  METHODS
  ELISA and PCR were used to study DC-SIGN binding properties and BSSL exon 11 size variation for human milk derived from 269 different mothers distributed over 4 geographical regions.
  
  
  RESULTS
  DC-SIGN binding properties were highly variable for milks derived from different mothers and between samplings from different geographical regions. Differences in DC-SIGN binding were correlated with a genetic polymorphism in BSSL which is related to the number of 11 amino acid repeats at the C-terminus of the protein.
  
  
  CONCLUSIONS
  The observed variation in DC-SIGN binding properties among milk samples may have implications for the risk of mucosal transmission of pathogens during breastfeeding.
authors.affiliation: Laboratory of Experimental Virology, Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
authors.forename: Martijn J
authors.initials: MJ
authors.lastname: Stax
authors.forename: Marloes A
authors.initials: MA
authors.lastname: Naarding
authors.forename: Michael W T
authors.initials: MW
authors.lastname: Tanck
authors.forename: Susanne
authors.initials: S
authors.lastname: Lindquist
authors.forename: Olle
authors.initials: O
authors.lastname: Hernell
authors.forename: Robert
authors.initials: R
authors.lastname: Lyle
authors.forename: Per
authors.initials: P
authors.lastname: Brandtzaeg
authors.forename: Merete
authors.initials: M
authors.lastname: Eggesbø
authors.forename: Georgios
authors.initials: G
authors.lastname: Pollakis
authors.forename: William A
authors.initials: WA
authors.lastname: Paxton
mesh_terms: D001942:Breast Feeding / Q000009:adverse effects; D015496:CD4-Positive T-Lymphocytes / Q000276:immunology / Q000378:metabolism / Q000821:virology; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D042622:DNA Repeat Expansion / Q000235:genetics / Q000502:physiology; D004534:Egypt; D005260:Female; D020022:Genetic Predisposition to Disease; D005838:Genotype; D015658:HIV Infections / Q000235:genetics* / Q000276:immunology / Q000378:metabolism / Q000635:transmission*; D015497:HIV-1 / Q000378:metabolism / Q000502:physiology; D006801:Humans; D007231:Infant, Newborn; D037181:Lectins, C-Type / Q000378:metabolism*; D008049:Lipase / Q000235:genetics* / Q000378:metabolism; D018811:Maternal Exposure / Q000009:adverse effects; D008895:Milk, Human / Q000378:metabolism* / Q000502:physiology / Q000821:virology; D009426:Netherlands; D009664:Norway; D011110:Polymorphism, Genetic / Q000502:physiology; D011485:Protein Binding / Q000235:genetics; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013548:Sweden; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D015815:Cell Adhesion Molecules; D037181:Lectins, C-Type; D008049:Lipase; D011956:Receptors, Cell Surface; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin; C054621:CEL protein, human